VDR_MOUSE
ID VDR_MOUSE Reviewed; 422 AA.
AC P48281; Q922X0;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Vitamin D3 receptor;
DE Short=VDR;
DE AltName: Full=1,25-dihydroxyvitamin D3 receptor;
DE AltName: Full=Nuclear receptor subfamily 1 group I member 1;
GN Name=Vdr; Synonyms=Nr1i1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7835717; DOI=10.1016/0378-1119(94)00735-b;
RA Kamei Y., Kawada T., Fukuwatari T., Ono T., Kato S., Sugimoto E.;
RT "Cloning and sequencing of the gene encoding the mouse vitamin D
RT receptor.";
RL Gene 152:281-282(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Intestine;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INDUCTION.
RX PubMed=14528024; DOI=10.1210/me.2003-0048;
RA Tsujikawa H., Kurotaki Y., Fujimori T., Fukuda K., Nabeshima Y.;
RT "Klotho, a gene related to a syndrome resembling human premature aging,
RT functions in a negative regulatory circuit of vitamin D endocrine system.";
RL Mol. Endocrinol. 17:2393-2403(2003).
RN [6]
RP INTERACTION WITH CRY1 AND CRY2.
RX PubMed=28751364; DOI=10.1073/pnas.1704955114;
RA Kriebs A., Jordan S.D., Soto E., Henriksson E., Sandate C.R., Vaughan M.E.,
RA Chan A.B., Duglan D., Papp S.J., Huber A.L., Afetian M.E., Yu R.T.,
RA Zhao X., Downes M., Evans R.M., Lamia K.A.;
RT "Circadian repressors CRY1 and CRY2 broadly interact with nuclear receptors
RT and modulate transcriptional activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:8776-8781(2017).
CC -!- FUNCTION: Nuclear receptor for calcitriol, the active form of vitamin
CC D3 which mediates the action of this vitamin on cells (By similarity).
CC Enters the nucleus upon vitamin D3 binding where it forms heterodimers
CC with the retinoid X receptor/RXR (By similarity). The VDR-RXR
CC heterodimers bind to specific response elements on DNA and activate the
CC transcription of vitamin D3-responsive target genes (By similarity).
CC Plays a central role in calcium homeostasis (By similarity).
CC {ECO:0000250|UniProtKB:P11473, ECO:0000250|UniProtKB:P13053}.
CC -!- SUBUNIT: Homodimer in the absence of bound vitamin D3. Heterodimer with
CC RXRA after vitamin D3 binding. Interacts with MED1, NCOA1, NCOA2, NCOA3
CC and NCOA6 coactivators, leading to a strong increase of transcription
CC of target genes. Interacts with the corepressor NCOR1. Interacts with
CC SNW1. Interacts with IRX4, the interaction does not affect its
CC transactivation activity (By similarity). Interacts with CRY1
CC (PubMed:28751364). Interacts with CRY2 in a ligand-dependent manner
CC (PubMed:28751364). {ECO:0000250|UniProtKB:P11473,
CC ECO:0000269|PubMed:28751364}.
CC -!- INTERACTION:
CC P48281; Q925T6: Grip1; NbExp=2; IntAct=EBI-346797, EBI-537752;
CC P48281; Q64337: Sqstm1; NbExp=3; IntAct=EBI-346797, EBI-645025;
CC P48281; Q00403: GTF2B; Xeno; NbExp=2; IntAct=EBI-346797, EBI-389564;
CC P48281; Q9Y6Q9: NCOA3; Xeno; NbExp=2; IntAct=EBI-346797, EBI-81196;
CC P48281; Q13573: SNW1; Xeno; NbExp=2; IntAct=EBI-346797, EBI-632715;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P11473,
CC ECO:0000255|PROSITE-ProRule:PRU00407}. Cytoplasm
CC {ECO:0000250|UniProtKB:P11473}. Note=Localizes mainly to the nucleus.
CC Translocated into the nucleus via both ligand-dependent and ligand-
CC independent pathways; ligand-independent nuclear translocation is
CC mediated by IPO4. {ECO:0000250|UniProtKB:P11473}.
CC -!- INDUCTION: By 1,25-dihydroxyvitamin D(3) in kidney.
CC {ECO:0000269|PubMed:14528024}.
CC -!- DOMAIN: Composed of three domains: a modulating N-terminal domain, a
CC DNA-binding domain and a C-terminal ligand-binding domain.
CC {ECO:0000250|UniProtKB:P11473}.
CC -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC number of yeast and animal transcription factors.
CC {ECO:0000250|UniProtKB:P11473}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC subfamily. {ECO:0000305}.
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DR EMBL; D31969; BAA06737.1; -; mRNA.
DR EMBL; AK030339; BAC26911.1; -; mRNA.
DR EMBL; AK154647; BAE32738.1; -; mRNA.
DR EMBL; CH466550; EDL04218.1; -; Genomic_DNA.
DR EMBL; BC006716; AAH06716.1; -; mRNA.
DR CCDS; CCDS27784.1; -.
DR PIR; PC4019; PC4019.
DR RefSeq; NP_033530.2; NM_009504.4.
DR AlphaFoldDB; P48281; -.
DR SMR; P48281; -.
DR BioGRID; 204511; 6.
DR ComplexPortal; CPX-673; RXRalpha-VDR nuclear hormone receptor complex.
DR ComplexPortal; CPX-872; RXRbeta-VDR nuclear hormone receptor complex.
DR CORUM; P48281; -.
DR DIP; DIP-31478N; -.
DR IntAct; P48281; 12.
DR MINT; P48281; -.
DR STRING; 10090.ENSMUSP00000023119; -.
DR BindingDB; P48281; -.
DR ChEMBL; CHEMBL5601; -.
DR iPTMnet; P48281; -.
DR PhosphoSitePlus; P48281; -.
DR MaxQB; P48281; -.
DR PaxDb; P48281; -.
DR PeptideAtlas; P48281; -.
DR PRIDE; P48281; -.
DR ProteomicsDB; 300197; -.
DR Antibodypedia; 3902; 818 antibodies from 44 providers.
DR DNASU; 22337; -.
DR Ensembl; ENSMUST00000023119; ENSMUSP00000023119; ENSMUSG00000022479.
DR GeneID; 22337; -.
DR KEGG; mmu:22337; -.
DR UCSC; uc007xlk.1; mouse.
DR CTD; 7421; -.
DR MGI; MGI:103076; Vdr.
DR VEuPathDB; HostDB:ENSMUSG00000022479; -.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000155473; -.
DR HOGENOM; CLU_007368_12_0_1; -.
DR InParanoid; P48281; -.
DR OMA; CITSPDM; -.
DR OrthoDB; 297114at2759; -.
DR PhylomeDB; P48281; -.
DR TreeFam; TF316304; -.
DR Reactome; R-MMU-196791; Vitamin D (calciferol) metabolism.
DR Reactome; R-MMU-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-MMU-4090294; SUMOylation of intracellular receptors.
DR BioGRID-ORCS; 22337; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Vdr; mouse.
DR PRO; PR:P48281; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P48281; protein.
DR Bgee; ENSMUSG00000022479; Expressed in duodenum and 137 other tissues.
DR ExpressionAtlas; P48281; baseline and differential.
DR Genevisible; P48281; MM.
DR GO; GO:0005901; C:caveola; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0001651; C:dense fibrillar component; ISO:MGI.
DR GO; GO:0000791; C:euchromatin; ISO:MGI.
DR GO; GO:0000792; C:heterochromatin; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016363; C:nuclear matrix; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI.
DR GO; GO:0030315; C:T-tubule; ISO:MGI.
DR GO; GO:1902098; F:calcitriol binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:1902121; F:lithocholic acid binding; ISO:MGI.
DR GO; GO:0038186; F:lithocholic acid receptor activity; ISO:MGI.
DR GO; GO:0004879; F:nuclear receptor activity; IDA:MGI.
DR GO; GO:0046965; F:nuclear retinoid X receptor binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0005499; F:vitamin D binding; ISO:MGI.
DR GO; GO:0070644; F:vitamin D response element binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
DR GO; GO:0060057; P:apoptotic process involved in mammary gland involution; IMP:MGI.
DR GO; GO:0097190; P:apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0038183; P:bile acid signaling pathway; ISO:MGI.
DR GO; GO:0006816; P:calcium ion transport; IMP:MGI.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0000902; P:cell morphogenesis; ISO:MGI.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:MGI.
DR GO; GO:0046697; P:decidualization; IEA:Ensembl.
DR GO; GO:0050892; P:intestinal absorption; IMP:MGI.
DR GO; GO:0007595; P:lactation; IMP:MGI.
DR GO; GO:0060745; P:mammary gland branching involved in pregnancy; IMP:MGI.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:1900155; P:negative regulation of bone trabecula formation; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0010839; P:negative regulation of keratinocyte proliferation; ISO:MGI.
DR GO; GO:0030279; P:negative regulation of ossification; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0060058; P:positive regulation of apoptotic process involved in mammary gland involution; IMP:MGI.
DR GO; GO:0030501; P:positive regulation of bone mineralization; IC:ComplexPortal.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0045618; P:positive regulation of keratinocyte differentiation; ISO:MGI.
DR GO; GO:2000830; P:positive regulation of parathyroid hormone secretion; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0010980; P:positive regulation of vitamin D 24-hydroxylase activity; ISO:MGI.
DR GO; GO:0070564; P:positive regulation of vitamin D receptor signaling pathway; ISO:MGI.
DR GO; GO:0060558; P:regulation of calcidiol 1-monooxygenase activity; IMP:BHF-UCL.
DR GO; GO:0051924; P:regulation of calcium ion transport; ISO:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0001501; P:skeletal system development; IMP:MGI.
DR GO; GO:0070561; P:vitamin D receptor signaling pathway; ISS:UniProtKB.
DR CDD; cd06955; NR_DBD_VDR; 1.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR InterPro; IPR042153; DBD_VDR.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR InterPro; IPR000324; VitD_rcpt.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PRINTS; PR00398; STRDHORMONER.
DR PRINTS; PR00047; STROIDFINGER.
DR PRINTS; PR00350; VITAMINDR.
DR SMART; SM00430; HOLI; 1.
DR SMART; SM00399; ZnF_C4; 1.
DR SUPFAM; SSF48508; SSF48508; 1.
DR PROSITE; PS51843; NR_LBD; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; DNA-binding; Metal-binding; Nucleus; Receptor;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..422
FT /note="Vitamin D3 receptor"
FT /id="PRO_0000053543"
FT DOMAIN 127..418
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 21..96
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 24..44
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 60..84
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 97..126
FT /note="Hinge"
FT /evidence="ECO:0000250|UniProtKB:P11473"
FT REGION 161..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..259
FT /note="Interaction with coactivator LXXLL motif"
FT /evidence="ECO:0000250|UniProtKB:P13053"
FT MOTIF 411..419
FT /note="9aaTAD"
FT /evidence="ECO:0000250|UniProtKB:P11473"
FT COMPBIAS 164..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 143
FT /ligand="calciol"
FT /ligand_id="ChEBI:CHEBI:28940"
FT /evidence="ECO:0000250|UniProtKB:P11473"
FT BINDING 222..232
FT /ligand="calciol"
FT /ligand_id="ChEBI:CHEBI:28940"
FT /evidence="ECO:0000250|UniProtKB:P11473"
FT BINDING 266..273
FT /ligand="calciol"
FT /ligand_id="ChEBI:CHEBI:28940"
FT /evidence="ECO:0000250|UniProtKB:P11473"
FT BINDING 300
FT /ligand="calciol"
FT /ligand_id="ChEBI:CHEBI:28940"
FT /evidence="ECO:0000250|UniProtKB:P11473"
FT BINDING 392
FT /ligand="calciol"
FT /ligand_id="ChEBI:CHEBI:28940"
FT /evidence="ECO:0000250|UniProtKB:P11473"
FT CONFLICT 276
FT /note="L -> M (in Ref. 1; BAA06737)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 422 AA; 47834 MW; 4614DD4A129F2732 CRC64;
MEAMAASTSL PDPGDFDRNV PRICGVCGDR ATGFHFNAMT CEGCKGFFRR SMKRKALFTC
PFNGDCRITK DNRRHCQACR LKRCVDIGMM KEFILTDEEV QRKREMIMKR KEEEALKDSL
RPKLSEEQQH IIAILLDAHH KTYDPTYADF RDFRPPIRAD VSTGSYSPRP TLSFSGDSSS
NSDLYTPSLD MMEPASFSTM DLNEEGSDDP SVTLDLSPLS MLPHLADLVS YSIQKVIGFA
KMIPGFRDLT SDDQIVLLKS SAIEVIMLRS NQSFTLDDMS WDCGSQDYKY DITDVSRAGH
TLELIEPLIK FQVGLKKLNL HEEEHVLLMA ICIVSPDRPG VQDAKLVEAI QDRLSNTLQT
YIRCRHPPPG SHQLYAKMIQ KLADLRSLNE EHSKQYRSLS FQPENSMKLT PLVLEVFGNE
IS
